1. Volume 32, Issue 2, Pages 265-275 (October 2001)
The Binding Site of Acetylcholine Receptor as Visualized in the X-Ray Structure of a Complex between α-Bungarotoxin and a Mimotope Peptide 
Michal Harel, Roni Kasher, Anne Nicolas, J.Mitchell Guss, Moshe Balass, Mati Fridkin, August B. Smit, Katjuša Brejc, Titia K. Sixma, Ephraim Katchalski-Katzir, Joel L. Sussman, Sara Fuchs 
Neuron 
Volume 32, Issue 2, Pages (October 2001)
DOI: /S (01)

2. Figure 1 Ramachandran Plot for α-BTX-HAP
The plot was produced by PROCHECK (Laskowski et al., 1993)
Neuron  , DOI: ( /S (01) )

3. Figure 2
The Crystallographic Packing of the α-BTX-HAP in the Crystal Produces Two Kinds of Dimers
(a) Monomer A makes a 2-fold related dimer with a continuous β sheet area across the 2-fold axis which is perpendicular to the plane of the β strands, like the one seen in the α-BTX X-ray structure (Protein Data Bank ID code 2abx) with the two HAPs situated far apart (ca. 40 Å) from each other. (b) Dimer produced by monomer B by a 2-fold axis which lies in the plane of the β strands. The two HAPs are likewise far apart
Neuron  , DOI: ( /S (01) )

4. Figure 3 3D Surface Drawing of the Structure of α-BTX-HAP
Color of the α-BTX corresponds to electrostatic charge, with blue positive and red negative (rendered with WebLabViewerLite software (MSI, 1998).
(a) α-BTX-HAP monomer A complex. HAP is shown in green.
(b) α-BTX monomer A with HAP removed
Neuron  , DOI: ( /S (01) )

5. Figure 4
The Snug Fit of Tyr189 of the HAP (Cyan) into a Loop Region of α-BTX (Yellow)
Short interactions shown as dashed lines. Water molecules shown in magenta. The composite omit map (Brünger et al., 1998) is drawn at 1.7σ
Neuron  , DOI: ( /S (01) )

6. Figure 5
Comparison, in Stereo, of the 3D Structures of HAP (Red) and Loop 182–193 of AChBP (Blue)
Only main chain and Cβ atoms are shown for clarity
Neuron  , DOI: ( /S (01) )

7. Figure 6
A Stereo View of the Combined Model of α-BTX-HAP (Red) and AChBP Structure with Subunit A in Green and Subunit B in Yellow Showing the Insertion of Loop 2 of the Toxin into the Interface of the Two Subunits
The positively charged HEPES molecule (black stick figure) shows the location of the acetylcholine binding site and the blockage of passage to this site caused by the binding of the toxin. The HAP, which overlaps the 182–193 loop of AChBP, is shown in blue
Neuron  , DOI: ( /S (01) )

8. Figure 7
The Combined Model of the AChBP Pentamer with Five Copies of α-BTX (Red) Bound to It, as Viewed down the 5-Fold Axis of the Pentamer
Neuron  , DOI: ( /S (01) )